HEADER HYDROLASE/HYDROLASE INHIBITOR 07-JUN-99 1CO7
TITLE R117H MUTANT RAT ANIONIC TRYPSIN COMPLEXED WITH BOVINE PANCREATIC
TITLE 2 TRYPSIN INHIBITOR (BPTI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN II;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.21.4;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BOVINE PANCREATIC TRYPSIN INHIBITOR;
COMPND 8 CHAIN: I;
COMPND 9 SYNONYM: BPTI
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: CATTLE;
SOURCE 8 ORGANISM_TAXID: 9913
KEYWDS COMPLEX (SERINE PROTEASE-INHIBITOR), HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.F.STAMPER,D.RINGE,L.HEDSTROM
REVDAT 4 04-APR-18 1CO7 1 REMARK
REVDAT 3 24-FEB-09 1CO7 1 VERSN
REVDAT 2 28-FEB-06 1CO7 1 JRNL REMARK
REVDAT 1 07-JAN-03 1CO7 0
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.9
REMARK 3 NUMBER OF REFLECTIONS : 21149
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2105
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2182
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 247
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.005
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1995
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.580
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CA.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : CA.TOP
REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CO7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000001155.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22249
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: 3TGI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.60400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 20.80200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 20.80200
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.60400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 COMPOUND
REMARK 400
REMARK 400 WARNING: SEQUENTIALLY DISTANT RESIDUE (I ASN 24 )
REMARK 400 AND RESIDUE (I LEU 29 ) ARE LINKED TOGETHER,
REMARK 400 DISTANCE ASN24I.C-LEU29I.N: 1.319A
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG E -6
REMARK 465 ALA E -5
REMARK 465 LEU E -4
REMARK 465 LEU E -3
REMARK 465 PHE E -2
REMARK 465 LEU E -1
REMARK 465 ALA E 0
REMARK 465 LEU E 1
REMARK 465 VAL E 2
REMARK 465 GLY E 3
REMARK 465 ALA E 4
REMARK 465 ALA E 5
REMARK 465 VAL E 6
REMARK 465 ALA E 7
REMARK 465 PHE E 8
REMARK 465 PRO E 9
REMARK 465 VAL E 10
REMARK 465 ASP E 11
REMARK 465 ASP E 12
REMARK 465 ASP E 13
REMARK 465 ASP E 14
REMARK 465 LYS E 15
REMARK 465 LYS I -33
REMARK 465 MET I -32
REMARK 465 SER I -31
REMARK 465 ARG I -30
REMARK 465 LEU I -29
REMARK 465 CYS I -28
REMARK 465 LEU I -27
REMARK 465 SER I -26
REMARK 465 VAL I -25
REMARK 465 ALA I -24
REMARK 465 LEU I -23
REMARK 465 LEU I -22
REMARK 465 VAL I -21
REMARK 465 LEU I -20
REMARK 465 LEU I -19
REMARK 465 GLY I -18
REMARK 465 THR I -17
REMARK 465 LEU I -16
REMARK 465 ALA I -15
REMARK 465 ALA I -14
REMARK 465 SER I -13
REMARK 465 THR I -12
REMARK 465 PRO I -11
REMARK 465 GLY I -10
REMARK 465 CYS I -9
REMARK 465 ASP I -8
REMARK 465 THR I -7
REMARK 465 SER I -6
REMARK 465 ASN I -5
REMARK 465 GLN I -4
REMARK 465 ALA I -3
REMARK 465 LYS I -2
REMARK 465 ALA I -1
REMARK 465 GLN I 0
REMARK 465 ARG I 1
REMARK 465 PRO I 2
REMARK 465 ASP I 3
REMARK 465 PHE I 4
REMARK 465 CYS I 5
REMARK 465 LEU I 6
REMARK 465 GLU I 7
REMARK 465 PRO I 8
REMARK 465 ALA I 25
REMARK 465 LYS I 26
REMARK 465 ALA I 27
REMARK 465 GLY I 28
REMARK 465 THR I 54
REMARK 465 CYS I 55
REMARK 465 GLY I 56
REMARK 465 GLY I 57
REMARK 465 ALA I 58
REMARK 465 ILE I 59
REMARK 465 GLY I 60
REMARK 465 PRO I 61
REMARK 465 TRP I 62
REMARK 465 GLU I 63
REMARK 465 ASN I 64
REMARK 465 LEU I 65
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG I 42 CB CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASN E 25 ND1 HIS E 117 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN I 24 N - CA - C ANGL. DEV. = -18.5 DEGREES
REMARK 500 LEU I 29 N - CA - C ANGL. DEV. = -32.8 DEGREES
REMARK 500 ARG I 53 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG I 53 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN E 25 47.85 30.01
REMARK 500 ASP E 49 -4.65 -55.51
REMARK 500 HIS E 71 -58.77 -134.91
REMARK 500 SER E 214 -66.92 -122.46
REMARK 500 ASN I 24 -50.81 -142.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 800 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 70 OE1
REMARK 620 2 ASN E 72 O 93.4
REMARK 620 3 VAL E 75 O 154.2 84.7
REMARK 620 4 GLU E 77 OE1 102.1 95.4 103.6
REMARK 620 5 GLU E 80 OE2 100.8 165.8 83.1 80.5
REMARK 620 6 HOH E 438 O 75.7 112.0 81.3 152.6 73.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE CATALYTIC TRIAD
REMARK 800
REMARK 800 SITE_IDENTIFIER: P1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE INHIBITOR RESIDUE IN THE PRIMARY SPECIFICITY
REMARK 800 SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 800
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 1CO7 E SWS P00763 -6 - 15 NOT IN ATOMS LIST
REMARK 999 1CO7 I SWS P00974 -33 - 8 NOT IN ATOMS LIST
REMARK 999 1CO7 I SWS P00974 25 - 28 NOT IN ATOMS LIST
REMARK 999 1CO7 I SWS P00974 54 - 65 NOT IN ATOMS LIST
REMARK 999
REMARK 999 WHILE SWISS-PROT NUMBERING IS CONSECUTIVE, PDB
REMARK 999 SEGMENT IS NUMBERED TO PROVIDE MAXIMUM HOMOLOGY
REMARK 999 WITH CHYMOTRYPSIN.
DBREF 1CO7 E -6 245 UNP P00763 TRY2_RAT 2 246
DBREF 1CO7 I -33 65 UNP P00974 BPT1_BOVIN 2 100
SEQADV 1CO7 HIS E 117 UNP P00763 ARG 121 VARIANT
SEQRES 1 E 245 ARG ALA LEU LEU PHE LEU ALA LEU VAL GLY ALA ALA VAL
SEQRES 2 E 245 ALA PHE PRO VAL ASP ASP ASP ASP LYS ILE VAL GLY GLY
SEQRES 3 E 245 TYR THR CYS GLN GLU ASN SER VAL PRO TYR GLN VAL SER
SEQRES 4 E 245 LEU ASN SER GLY TYR HIS PHE CYS GLY GLY SER LEU ILE
SEQRES 5 E 245 ASN ASP GLN TRP VAL VAL SER ALA ALA HIS CYS TYR LYS
SEQRES 6 E 245 SER ARG ILE GLN VAL ARG LEU GLY GLU HIS ASN ILE ASN
SEQRES 7 E 245 VAL LEU GLU GLY ASN GLU GLN PHE VAL ASN ALA ALA LYS
SEQRES 8 E 245 ILE ILE LYS HIS PRO ASN PHE ASP ARG LYS THR LEU ASN
SEQRES 9 E 245 ASN ASP ILE MET LEU ILE LYS LEU SER SER PRO VAL LYS
SEQRES 10 E 245 LEU ASN ALA HIS VAL ALA THR VAL ALA LEU PRO SER SER
SEQRES 11 E 245 CYS ALA PRO ALA GLY THR GLN CYS LEU ILE SER GLY TRP
SEQRES 12 E 245 GLY ASN THR LEU SER SER GLY VAL ASN GLU PRO ASP LEU
SEQRES 13 E 245 LEU GLN CYS LEU ASP ALA PRO LEU LEU PRO GLN ALA ASP
SEQRES 14 E 245 CYS GLU ALA SER TYR PRO GLY LYS ILE THR ASP ASN MET
SEQRES 15 E 245 VAL CYS VAL GLY PHE LEU GLU GLY GLY LYS ASP SER CYS
SEQRES 16 E 245 GLN GLY ASP SER GLY GLY PRO VAL VAL CYS ASN GLY GLU
SEQRES 17 E 245 LEU GLN GLY ILE VAL SER TRP GLY TYR GLY CYS ALA LEU
SEQRES 18 E 245 PRO ASP ASN PRO GLY VAL TYR THR LYS VAL CYS ASN TYR
SEQRES 19 E 245 VAL ASP TRP ILE GLN ASP THR ILE ALA ALA ASN
SEQRES 1 I 99 LYS MET SER ARG LEU CYS LEU SER VAL ALA LEU LEU VAL
SEQRES 2 I 99 LEU LEU GLY THR LEU ALA ALA SER THR PRO GLY CYS ASP
SEQRES 3 I 99 THR SER ASN GLN ALA LYS ALA GLN ARG PRO ASP PHE CYS
SEQRES 4 I 99 LEU GLU PRO PRO TYR THR GLY PRO CYS LYS ALA ARG ILE
SEQRES 5 I 99 ILE ARG TYR PHE TYR ASN ALA LYS ALA GLY LEU CYS GLN
SEQRES 6 I 99 THR PHE VAL TYR GLY GLY CYS ARG ALA LYS ARG ASN ASN
SEQRES 7 I 99 PHE LYS SER ALA GLU ASP CYS MET ARG THR CYS GLY GLY
SEQRES 8 I 99 ALA ILE GLY PRO TRP GLU ASN LEU
HET CA E 800 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
FORMUL 4 HOH *103(H2 O)
HELIX 1 1 ALA E 56 CYS E 58 5 3
HELIX 2 2 GLN E 165 SER E 171 1 7
HELIX 3 3 VAL E 231 ASN E 233 5 3
HELIX 4 4 VAL E 235 ALA E 243 1 9
HELIX 5 5 ALA I 48 CYS I 51 1 4
SHEET 1 A 7 GLN E 81 ASN E 84 0
SHEET 2 A 7 GLN E 64 LEU E 68 -1 N LEU E 68 O GLN E 81
SHEET 3 A 7 GLN E 30 ASN E 34 -1 N ASN E 34 O GLN E 64
SHEET 4 A 7 HIS E 40 ASN E 48 -1 N GLY E 44 O VAL E 31
SHEET 5 A 7 TRP E 51 SER E 54 -1 N VAL E 53 O SER E 45
SHEET 6 A 7 MET E 104 LEU E 108 -1 N ILE E 106 O VAL E 52
SHEET 7 A 7 ALA E 85 LYS E 90 -1 N ILE E 89 O LEU E 105
SHEET 1 B 2 GLN E 135 GLY E 140 0
SHEET 2 B 2 GLN E 156 PRO E 161 -1 N ALA E 160 O CYS E 136
SHEET 1 C 4 MET E 180 VAL E 183 0
SHEET 2 C 4 GLY E 226 LYS E 230 -1 N TYR E 228 O VAL E 181
SHEET 3 C 4 GLU E 204 TRP E 215 -1 N TRP E 215 O VAL E 227
SHEET 4 C 4 PRO E 198 CYS E 201 -1 N CYS E 201 O GLU E 204
SHEET 1 D 2 ILE I 18 PHE I 22 0
SHEET 2 D 2 GLN I 31 TYR I 35 -1 N TYR I 35 O ILE I 18
SSBOND 1 CYS E 22 CYS E 157 1555 1555 2.04
SSBOND 2 CYS E 42 CYS E 58 1555 1555 2.03
SSBOND 3 CYS E 128 CYS E 232 1555 1555 2.03
SSBOND 4 CYS E 136 CYS E 201 1555 1555 2.02
SSBOND 5 CYS E 168 CYS E 182 1555 1555 2.02
SSBOND 6 CYS E 191 CYS E 220 1555 1555 2.03
SSBOND 7 CYS I 14 CYS I 38 1555 1555 2.04
SSBOND 8 CYS I 30 CYS I 51 1555 1555 2.03
LINK OE1 GLU E 70 CA CA E 800 1555 1555 2.44
LINK O ASN E 72 CA CA E 800 1555 1555 2.34
LINK O VAL E 75 CA CA E 800 1555 1555 2.29
LINK OE1 GLU E 77 CA CA E 800 1555 1555 2.60
LINK OE2 GLU E 80 CA CA E 800 1555 1555 2.46
LINK CA CA E 800 O HOH E 438 1555 1555 3.03
SITE 1 CAT 3 HIS E 57 ASP E 102 SER E 195
SITE 1 P1 1 LYS I 15
SITE 1 AC1 6 GLU E 70 ASN E 72 VAL E 75 GLU E 77
SITE 2 AC1 6 GLU E 80 HOH E 438
CRYST1 92.696 92.696 62.406 90.00 90.00 120.00 P 32 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010788 0.006228 0.000000 0.00000
SCALE2 0.000000 0.012457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016024 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
